Bovine neurophysins I and I1 have been obtained in a highly purified state using isoelectric focusing. The interactions of oxytocin and [8-lysine]vasopressin with these proteins have been investigated by thin-film equilibrium dialysis using highly radioactive hormones retaining their full biological activities. I n this report, we present the results of binding studies carried out using the equilibrium dialysis technique with highly purified neurophysins obtained by isoelectric focusing of crude protein material. The thermodynamic parameters and the stoichiometry of the reaction between the hormones and the proteins have been established. These findings are discussed in terms of the molecular mechanisms by which the neurophysins bind to the hormonal peptides.
Using gel retardation and DNase I protection techniques, we have demonstrated that the Escherichia coli integration host factor (IHF) stabilizes the interaction between Mu repressor and its cognate operator-binding sites in vitro. These results are discussed in terms of a model in which IHF may commit the phage to the lytic or lysogenic pathway depending on the occupancy of the operator sites by the repressor.
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